1NIR
OXYDIZED NITRITE REDUCTASE FROM PSEUDOMONAS AERUGINOSA
Summary for 1NIR
Entry DOI | 10.2210/pdb1nir/pdb |
Descriptor | NITRITE REDUCTASE, PHOSPHATE ION, CHLORIDE ION, ... (7 entities in total) |
Functional Keywords | nitrite reductase, pseudomonas aeruginosa, hemoprotein, denitrification, domain swapping |
Biological source | Pseudomonas aeruginosa |
Cellular location | Periplasm: P24474 |
Total number of polymer chains | 2 |
Total formula weight | 123474.94 |
Authors | Nurizzo, D.,Tegoni, M.,Cambillau, C. (deposition date: 1997-06-17, release date: 1997-12-03, Last modification date: 2024-10-16) |
Primary citation | Nurizzo, D.,Silvestrini, M.C.,Mathieu, M.,Cutruzzola, F.,Bourgeois, D.,Fulop, V.,Hajdu, J.,Brunori, M.,Tegoni, M.,Cambillau, C. N-terminal arm exchange is observed in the 2.15 A crystal structure of oxidized nitrite reductase from Pseudomonas aeruginosa. Structure, 5:1157-1171, 1997 Cited by PubMed Abstract: Nitrite reductase from Pseudomonas aeruginosa (NiR-Pa) is a dimer consisting of two identical 60 kDa subunits, each of which contains one c and one d1 heme group. This enzyme, a soluble component of the electron-transfer chain that uses nitrate as a source of energy, can be induced by the addition of nitrate to the bacterial growth medium. NiR-Pa catalyzes the reduction of nitrite (NO2-) to nitric oxide (NO); in vitro, both cytochrome c551 and azurin are efficient electron donors in this reaction. NiR is a key denitrification enzyme, which controls the rate of the production of toxic nitric oxide (NO) and ultimately regulates the release of NO into the atmosphere. PubMed: 9331415DOI: 10.1016/S0969-2126(97)00267-0 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.15 Å) |
Structure validation
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